ID   PUR8_SPICI              Reviewed;          88 AA.
AC   P52201;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Adenylosuccinate lyase;
DE            Short=ASL;
DE            EC=4.3.2.2 {ECO:0000250|UniProtKB:P0AB89};
DE   AltName: Full=Adenylosuccinase;
DE            Short=ASase;
DE   Flags: Fragment;
GN   Name=purB;
OS   Spiroplasma citri.
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC   Spiroplasma.
OX   NCBI_TaxID=2133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=R8A2HP;
RA   Citti C., Saillard C., Bove J.M.;
RL   Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes two reactions in de novo purine nucleotide
CC       biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-
CC       succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-
CC       D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-
CC       carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-
CC       ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate
CC       (ADS or N(6)-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP)
CC       and fumarate. {ECO:0000250|UniProtKB:P0AB89}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate;
CC         Xref=Rhea:RHEA:16853, ChEBI:CHEBI:29806, ChEBI:CHEBI:57567,
CC         ChEBI:CHEBI:456215; EC=4.3.2.2;
CC         Evidence={ECO:0000250|UniProtKB:P0AB89};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16854;
CC         Evidence={ECO:0000250|UniProtKB:P0AB89};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-
CC         carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide + fumarate; Xref=Rhea:RHEA:23920,
CC         ChEBI:CHEBI:29806, ChEBI:CHEBI:58443, ChEBI:CHEBI:58475; EC=4.3.2.2;
CC         Evidence={ECO:0000250|UniProtKB:P0AB89};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23921;
CC         Evidence={ECO:0000250|UniProtKB:P0AB89};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC       from IMP: step 2/2.
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC       amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC       phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC   -!- SUBUNIT: Homotetramer and homodimer. Residues from neighboring subunits
CC       contribute catalytic and substrate-binding residues to each active site
CC       (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L22971; AAA26587.1; -; Genomic_DNA.
DR   AlphaFoldDB; P52201; -.
DR   SMR; P52201; -.
DR   STRING; 2133.SCITRI_00275; -.
DR   UniPathway; UPA00074; UER00132.
DR   UniPathway; UPA00075; UER00336.
DR   GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.275.10; -; 1.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   SUPFAM; SSF48557; SSF48557; 1.
PE   3: Inferred from homology;
KW   Lyase; Purine biosynthesis.
FT   CHAIN           1..>88
FT                   /note="Adenylosuccinate lyase"
FT                   /id="PRO_0000137883"
FT   BINDING         4..5
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   BINDING         67..69
FT                   /ligand="N(6)-(1,2-dicarboxyethyl)-AMP"
FT                   /ligand_id="ChEBI:CHEBI:57567"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB89"
FT   NON_TER         88
SQ   SEQUENCE   88 AA;  10264 MW;  2C3FB0BB1FD2829F CRC64;
     MIERYFVTEI GKIWSDENKY NTWAKVELLV CEGWAQIGLI PPTDIEKIKT NLTVNLPRML
     ELEAETKHDV VAFTRMLSET LGPEKKWI